4nsx

Crystal Structure of the Utp21 tandem WD Domain

spinqualitylabelsall models 4nsx, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nsx is a 1 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FLC Gene: L8084.22, UTP21, YLR409C (Baker's yeast) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [UTP21_YEAST] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Publication Abstract from PubMed Assembly of the eukaryotic ribosome requires a large number of trans-acting proteins and small nucleolar RNAs that transiently associate with the precursor rRNA to facilitate its modification, processing and binding with ribosomal proteins. UTPB is a large evolutionarily conserved complex in the 90S small subunit processome that mediates early processing of 18S rRNA. UTPB consists of six proteins Utp1/Pwp1, Utp6, Utp12/Dip2, Utp13, Utp18 and Utp21 and has abundant WD domains. Here, we determined the crystal structure of the tandem WD domain of yeast Utp21 at 2.1 A resolution, revealing two open-clamshell-shaped beta-propellers. The bottom faces of both WD domains harbor several conserved patches that potentially function as molecular binding sites. We show that residues 100-190 of Utp18 bind to the tandem WD domain of Utp21. Structural mapping of previous crosslinking data shows that the WD domains of Utp18 and Utp1 are organized on two opposite sides of the Utp21 WD domains. This study reports the first structure of a UTPB component and provides insight into the structural organization of the UTPB complex. Structure of Utp21 Tandem WD Domain Provides Insight into the Organization of the UTPB Complex Involved in Ribosome Synthesis.,Zhang C, Lin J, Liu W, Chen X, Chen R, Ye K PLoS One. 2014 Jan 21;9(1):e86540. doi: 10.1371/journal.pone.0086540. eCollection, 2014 Jan 21. PMID:24466140 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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